콩 단백질은 글리시닌과 β-콘글리시닌을 주요 성분으로 하며, 콩 β-콘글리시닌이 나타내는 알레르기 원인과 콜레스테롤 저하 작용을 밝히고저 유전자 공학적인 방법을 시도하였다. 즉 β-콘글리시닌의 α-subunit를 유전자 클로닝하고 대장균에서의 발현시스템을 구축하였다. 발현벡터는 pET21d이며 플라스미드를 구축하여 E. coli BL21(DE3)에 형질전환시켰고 발현된 단백질은 균체전체 단백질의 15%이며 90%이상이 가용화 상태로 축적되었다. 축적된 발현 단백질은 천연의 β-콘글리시닌과 동일한 트리머로 확인되었다. 발현 단백질은 20∼40% 황산암모늄 분별침전과 Q-Sepharose 이온교환크로마토그래피, Butyltoyopearl 소수성 컬럼크로마토그래피로 정제하였다. 이것은 콩단백질의 기능특성을 규명하는데 필요한 대장균 대량 발현계를 확립하고 발현 단백질의 정제방법을 확립한 결과이다.

Antibodies raised against the purified p-subunit of β -conglycinin were used in immunohistochemical studies to monitor the pattern of β -conglycinin mobilization in the cotyledons during soybean [Glycine max (L.) Merr.] seed germination. Western blot analysis revealed that the break down of the β -subunit of β -conglycinin commenced as early as 2 days after seed imbibition (DAI). Concurrent with the degradation of the β -subunit of β -conglycinin, accumulation of 48, 28, and 26 kD proteolytic intermediates was observed from 2 to 6 DAI. Western blot analysis also revealed that the acidic subunit of glycinin was mobilized earlier than the basic subunit. The basic glycinin subunit was subjected to proteolysis within 2 DAI resulting in the appearance of an intermediate product approximately 2 kD smaller than the native basic glycinin subunit. In contrast to the major seed storage proteins, lipoxygenase was subjected to limited proteolysis and was detected even after 8 DAI. The first sign of β -conglycinin breakdown was observed near the vascular strands and proceeded from the vascular strands towards the epidermis. Protein A-gold localization studies using thin sections of soybean cotyledons and antibodies raised against the β -subunit of β -conglycinin revealed intense labeling over protein bodies. A pronounced decrease in the protein A-gold labeling intensity over protein bodies was observed at later stages of seed germination. The protein bodies, which were converted into a large central vacuole by 8 DAI, contained very little 7S protein as evidenced by sparse protein A-gold labeling in the vacuoles.